TFB2M_DROME
ID TFB2M_DROME Reviewed; 452 AA.
AC Q9VH38; Q95SS3;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Dimethyladenosine transferase 2, mitochondrial;
DE EC=2.1.1.-;
DE AltName: Full=Mitochondrial 12S rRNA dimethylase 2;
DE AltName: Full=Mitochondrial transcription factor B2;
DE AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2;
DE AltName: Full=d-mtTFB2;
DE Flags: Precursor;
GN Name=mtTFB2; ORFNames=CG3910;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15060065; DOI=10.1074/jbc.m401643200;
RA Matsushima Y., Garesse R., Kaguni L.S.;
RT "Drosophila mitochondrial transcription factor B2 regulates mitochondrial
RT DNA copy number and transcription in schneider cells.";
RL J. Biol. Chem. 279:26900-26905(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase
CC which specifically dimethylates mitochondrial 12S rRNA at the conserved
CC stem loop. Also required for basal transcription of mitochondrial DNA.
CC Also regulates mitochondrial DNA copy number. Stimulates transcription
CC independently of the methyltransferase activity.
CC {ECO:0000269|PubMed:15060065}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15060065}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. rRNA adenine N(6)-methyltransferase family. KsgA
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01026}.
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DR EMBL; AY508412; AAS91579.1; -; mRNA.
DR EMBL; AE014297; AAF54482.2; -; Genomic_DNA.
DR EMBL; AY060616; AAL28164.1; -; mRNA.
DR RefSeq; NP_649971.1; NM_141714.4.
DR AlphaFoldDB; Q9VH38; -.
DR SMR; Q9VH38; -.
DR STRING; 7227.FBpp0081651; -.
DR PaxDb; Q9VH38; -.
DR PRIDE; Q9VH38; -.
DR DNASU; 41228; -.
DR EnsemblMetazoa; FBtr0082173; FBpp0081651; FBgn0037778.
DR GeneID; 41228; -.
DR KEGG; dme:Dmel_CG3910; -.
DR CTD; 41228; -.
DR FlyBase; FBgn0037778; mtTFB2.
DR VEuPathDB; VectorBase:FBgn0037778; -.
DR eggNOG; ENOG502S0IT; Eukaryota.
DR HOGENOM; CLU_043862_0_0_1; -.
DR InParanoid; Q9VH38; -.
DR OMA; RAQACKK; -.
DR OrthoDB; 1169941at2759; -.
DR PhylomeDB; Q9VH38; -.
DR Reactome; R-DME-163282; Mitochondrial transcription initiation.
DR BioGRID-ORCS; 41228; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41228; -.
DR PRO; PR:Q9VH38; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037778; Expressed in eye disc (Drosophila) and 21 other tissues.
DR Genevisible; Q9VH38; DM.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0034246; F:mitochondrial transcription factor activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0006390; P:mitochondrial transcription; IMP:FlyBase.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
DR GO; GO:0006391; P:transcription initiation from mitochondrial promoter; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001737; KsgA/Erm.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016861; TFB2M.
DR PANTHER; PTHR11727; PTHR11727; 1.
DR PANTHER; PTHR11727:SF13; PTHR11727:SF13; 1.
DR Pfam; PF00398; RrnaAD; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; Mitochondrion; Reference proteome; RNA-binding;
KW rRNA processing; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..452
FT /note="Dimethyladenosine transferase 2, mitochondrial"
FT /id="PRO_0000273185"
FT REGION 408..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..434
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 99
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 125
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 452 AA; 52175 MW; 1DF9A7FB3F1826F2 CRC64;
MLPLRCSWSF ARANYSTKKE LVTRYSGDFP EKLLNRKQKV PTHMYIANSE AAARINQYLE
PHFQSSGCDT VMELNSGAGY FTRHLLDRES QFRRIILLES MDHFMPKIQE LHTLYPERVK
VRQGDFVNLW KLVYMDKMDG GSRVADLLSD VPQKAFTDDI NMLVFGAVGS YPFFKHLINS
LIFQTSLFNL GRCEMILAMP PPIYIHLTCN NEIGYLIYRS TSVLFQILFE HKFIAKVPRE
DFLPQQMAYS PTKSSKLGKV QSINPEYLYL VKFTPRRNLH ELCQSQDLPA LWFFIKQNYV
SRRNRIIPNL EKWVPGCGPR LIINPKSSES VTPIYPDELP KKLPQYSCQS TTMSTRNYYP
GINIYTQFGD LLPSQILTLF SQFRQWPEYG ESSFLASLEN ALLKLETAND EPNLEDGVTL
PEEDDAEADE IIEEESPVPA TTPVKRRRKA SS
